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  Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase

Monnat, J., Neuhaus, E. M., Pop, M. S., Ferrari, D. M., Kramer, B., & Soldati, T. (2000). Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase. Molecular Biology of the Cell, 11(10), 3469-3484. doi:10.1091/mbc.11.10.3469.

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Genre: Journal Article
Alternative Title : Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium rotein disulfide isomerase

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Monnat, Jean1, Author              
Neuhaus, Eva Maria1, Author              
Pop, Marius S., Author
Ferrari, David M., Author
Kramer, Barbara, Author
Soldati, Thierry, Author              
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1Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

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 Abstract: Localization of soluble endoplasmic reticulum (ER) resident proteins is likely achieved by the complementary action of retrieval and retention mechanisms. Whereas the machinery involving the H/KDEL and related retrieval signals in targeting escapees back to the ER is well characterized, other mechanisms including retention are still poorly understood. We have identified a protein disulfide isomerase (Dd-PDI) lacking the HDEL retrieval signal normally found at the C terminus of ER residents in Dictyostelium discoideum. Here we demonstrate that its 57 residue C-terminal domain is necessary for intracellular retention of Dd-PDI and sufficient to localize a green fluorescent protein (GFP) chimera to the ER, especially to the nuclear envelope. Dd-PDI and GFP-PDI57 are recovered in similar cation-dependent complexes. The overexpression of GFP-PDI57 leads to disruption of endogenous PDI complexes and induces the secretion of PDI, whereas overexpression of a GFP-HDEL chimera induces the secretion of endogenous calreticulin, revealing the presence of two independent and saturable mechanisms. Finally, low-level expression of Dd-PDI but not of PDI truncated of its 57 C-terminal residues complements the otherwise lethal yeast TRG1/PDI1 null mutation, demonstrating functional disulfide isomerase activity and ER localization. Altogether, these results indicate that the PDI57 peptide contains ER localization determinants recognized by a conserved machinery present in D. discoideum and Saccharomyces cerevisiae

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Language(s): eng - English
 Dates: 1999-10-042000-07-282000-10
 Publication Status: Published in print
 Pages: 16
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 Rev. Type: Peer
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Title: Molecular Biology of the Cell
  Other : Mol. Biol. Cell
Source Genre: Journal
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Publ. Info: American Society for Cell Biology
Pages: - Volume / Issue: 11 (10) Sequence Number: - Start / End Page: 3469 - 3484 Identifier: ISSN: 1059-1524
CoNE: https://pure.mpg.de/cone/journals/resource/954927716372_1